ID C6DK21_PECCP Unreviewed; 890 AA.
AC C6DK21;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN OrderedLocusNames=PC1_2373 {ECO:0000313|EMBL:ACT13404.1};
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13404.1, ECO:0000313|Proteomes:UP000002736};
RN [1] {ECO:0000313|EMBL:ACT13404.1, ECO:0000313|Proteomes:UP000002736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1 {ECO:0000313|EMBL:ACT13404.1,
RC ECO:0000313|Proteomes:UP000002736};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501,
CC ECO:0000256|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP001657; ACT13404.1; -; Genomic_DNA.
DR RefSeq; WP_015840586.1; NC_012917.1.
DR AlphaFoldDB; C6DK21; -.
DR STRING; 561230.PC1_2373; -.
DR KEGG; pct:PC1_2373; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 76..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 691..818
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 97815 MW; A5ED2F9212DED3A1 CRC64;
MSSHLRDTCL DTLTVQQQIY HYYSLPKAAK TLGNIDKLPK SLKVLLENLL RHQDGDTVEQ
DDLQAVVDWL KTGHVDREIA YRPARVLMQD FTGVPAVVDL AAMRAAVKRL GGDVNKVNPL
SPVDLVIDHS VTVDHFGDRQ ALTDNTQLEM ARNRERYEFL RWGQNAFSHF SVVPPGTGIC
HQVNLEYLAK AIWYEKQGDK QFAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPDVV GVKLSGKMRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR
ATIANMAPEY GATCGFFPID QITLDYMRLT NRAEEQIALV EAYSKQQGLW RNTGDEPVFT
SQLALDLATV ETSLAGPKRP QDRVPLAGVP EAFKASRELD VSTVKNRSDY EEFTLEGETH
RLQQGAVVIA AITSCTNTSN PSVLMTAGLL AKNAVERGLK TKPWVKTSLA PGSRVVTDYY
AKAGLTTYLD ALGFNLVGYG CTTCIGNSGP LPDAIEAAIK AGDLTVGAVL SGNRNFEGRI
HPLVKTNWLA SPPLVVAYAL AGNMNVDLTQ EPLGEDRDGK AVYLKDIWPS TKAVADAVLN
VSAGMFHKQY AAVFEGTQEW QDIEVDDNPT YQWPEESTYI RQTPFFLDMG KEPEPVQDIH
KARILAMLGD SVTTDHISPA GNIKRDSPAG KYLLERGVET AEFNSYGSRR GNHEVMMRGT
FANIRIRNEM VPGKEGGYTR HIPSQNEMTI YDAAMRYKDD NVPLALFAGK EYGSGSSRDW
AAKGPRLLGV RVVIAESFER IHRSNLIGMG ILPLEFPEGV TRKTLQLTGD EQISITGLNQ
LTPGATVEVN ITDASGNTQA ISTRCRIDTR NELTYYQNDG ILHYVIRNML
//
